Literature summary for 1.5.1.11 extracted from

  • Monneuse-Doublet, M.O.; Lefebure, F.; Olomucki, A.
    Isolation and characterization of two molecular forms of octopine dehydrogenase from Pecten maximus L. (1980), Eur. J. Biochem., 108, 261-269.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information
-
Pecten maximus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
43000
-
1 * 43000, enzyme form A and B, SDS-PAGE Pecten maximus

Organism

Organism UniProt Comment Textmining
Pecten maximus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Pecten maximus

Source Tissue

Source Tissue Comment Organism Textmining
adductor striated adductor muscle, 2 enzyme form A and B Pecten maximus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Pecten maximus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Arg + pyruvate + NADH
-
Pecten maximus N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
?

Subunits

Subunits Comment Organism
monomer 1 * 43000, enzyme form A and B, SDS-PAGE Pecten maximus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
41
-
half-denaturation time: 40 min, enzyme forms A and B Pecten maximus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
enzyme form A and B, octopine formation Pecten maximus
9.7
-
enzyme form A and B, octopine oxidation Pecten maximus

pH Stability

pH Stability pH Stability Maximum Comment Organism
additional information
-
enzyme form B is more sensitive to alkaline treatments than enzyme form A Pecten maximus

Cofactor

Cofactor Comment Organism Structure
NADH
-
Pecten maximus